ProGP390 (Putative sulfatase protein)
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ProGP ID | ProGP390 (Putative sulfatase protein) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Campylobacter jejuni HB93-13 |
Domain | Bacteria |
Classification | Phylum : Proteobacteria Class : Epsilonproteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : jejuni Subspecies : jejuni Strain : HB93-13 |
Taxonomic ID (NCBI) | 192222 |
Genome Information | |
GenBank | NC_002163.1 |
EMBL | AL111168 |
Organism Additional Information | Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity. |
Gene Information | |
Gene Name | cj1055c |
NCBI Gene ID | 905347 |
GenBank Gene Sequence | NC_002163.1. |
Protein Information | |
Protein Name | Putative sulfatase protein |
UniProtKB/SwissProt ID | Q0P9J7 |
NCBI RefSeq | WP_010891905.1 |
EMBL-CDS | CAL35173.1 |
UniProtKB Sequence | >tr|Q0P9J7|Q0P9J7_CAMJE Putative sulfatase family protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj1055c PE=4 SV=1 MRKILLQIFIFSVLFIATFAINRILMQNSFIPTGLISDKNEIFLMYLLGVFHDIRFLSAA FLPFLLCGFLSLIFSNIKINNKLVIYSKNFYFIFSSVYIIVLSCLCIGFSYVKYYYYEIY KTKFDIFMFTLKDDNTKTILSIIYHDYPILKILALMLIFGVFVFFLNLKILNLKLKPVNL RLFPLIALNLILIIVYVIALRGPFKHVAINVQNYSFSEYSVVNDTMLNPIMAFSWALKQY KEEAALKVITPLKAQELKEKLFDYLHQSPINLKAEKNHPSVFVNLMESFGLNLADFTNTE HNFLGSLDKHFKQDFLFKRFLSSSNGTIPSFANLFFVSPFSNISTSKFQKTYLDLTPIAV YKKAGYKVIFVSAGNGSWQNIKNYLSILGVDEIIDENILMKEYNGAKDSENGYGIADEFL YKKVYDLLQKNPHKTLIIALTISNHPPYKIPQNDLPKLQNIPQTLLNMLPYEKDKQDNII KAYTYANNEFGKFLDKVKQSPFKNSVIIAATGDHRVREMSMDLNSQKAFAYSVPFYLYIP KDLQDNIYYDKDRVGSHKDIFPTLYALSLNNVKYLSVGGRNMLARPSDEKLEFGINDAVW IDKKGIYSGGKGYYFESNDTLKDMNKAFNLDGYTKDFDKFYRELNLYQLAERLGISK |
Sequence length | 657 AA |
Glycosylation Status | |
Glycosylation Type | N- (Asn) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | N618 |
Glycosite(s) Annotated Protein Sequence | >tr|Q0P9J7|Q0P9J7_CAMJE Putative sulfatase family protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj1055c PE=4 SV=1 MRKILLQIFIFSVLFIATFAINRILMQNSFIPTGLISDKNEIFLMYLLGVFHDIRFLSAA FLPFLLCGFLSLIFSNIKINNKLVIYSKNFYFIFSSVYIIVLSCLCIGFSYVKYYYYEIY KTKFDIFMFTLKDDNTKTILSIIYHDYPILKILALMLIFGVFVFFLNLKILNLKLKPVNL RLFPLIALNLILIIVYVIALRGPFKHVAINVQNYSFSEYSVVNDTMLNPIMAFSWALKQY KEEAALKVITPLKAQELKEKLFDYLHQSPINLKAEKNHPSVFVNLMESFGLNLADFTNTE HNFLGSLDKHFKQDFLFKRFLSSSNGTIPSFANLFFVSPFSNISTSKFQKTYLDLTPIAV YKKAGYKVIFVSAGNGSWQNIKNYLSILGVDEIIDENILMKEYNGAKDSENGYGIADEFL YKKVYDLLQKNPHKTLIIALTISNHPPYKIPQNDLPKLQNIPQTLLNMLPYEKDKQDNII KAYTYANNEFGKFLDKVKQSPFKNSVIIAATGDHRVREMSMDLNSQKAFAYSVPFYLYIP KDLQDNIYYDKDRVGSHKDIFPTLYALSLNNVKYLSVGGRNMLARPSDEKLEFGINDAVW IDKKGIYSGGKGYYFESN*(618)DTLKDMNKAFNLDGYTKDFDKFYRELNLYQLAERLGISK |
Sequence Around Glycosites (21 AA) | SGGKGYYFESNDTLKDMNKAF |
Technique(s) used for Glycosylation Detection | ZIC-HILIC enrichment |
Technique(s) used for Glycosylated Residue(s) Detection | Reversed Phase LC-Tandem CID/HCD-MS |
Glycan Information | |
Glycan Annotation | Heptasaccharide GalNAc- α1,4-GalNAc- α1,4-(Glcβ1,3)-GalNAc- α1,4-GalNAc- α1,4-GalNAc- α1,3-Bac-β1 where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucopyranose) |
BCSDB ID | 20059 |
GlyTouCan | G38348FF |
Technique(s) used for Glycan Identification | Reversed Phase LC-Tandem CID/HCD-MS |
Literature | |
Year of Identification | 2011 |
Year of Identification Month Wise | 2011.2.10 |
Year of Validation | 2011 |
Reference | Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S.P., Højrup, P. and Packer, N.H., 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Molecular & cellular proteomics, 10(2), pp.S1-S18. |
Corresponding Author | Stuart J Cordwell |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |